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Journal articles on the topic 'Monoclonial antibodies'

Author: Grafiati

Published: 4 June 2021

Last updated: 19 February 2022

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1

Мерзляк, Е. М., Д. С. Сырко, Е. А. Мусаткина, and М. А. Израельсон. "Использование моноклональных антител для терапии аутоиммунных заболеваний." НАНОМЕДИЦИНА, no. 6 (December 31, 2018): 164–69. http://dx.doi.org/10.24075/vrgmu.2018.094.

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В последнее время в терапии аутоиммунных заболеваний стали применять моноклональные антитела. Мишенью этих антител являются провоспалительные цитокины и собственно Т и В-клетки потенциально участвующие в патогенезе заболевания. В данной статье проведена попытка систематизировать используемые препараты и привести основные механизмы, лежащие в основе такого рода терапии, описаны нежелательные побочные действия. Потенциальными путями и перспективами развития биологиксов в лечении аутоиммунных заболеваний, по нашему мнению, являются моноклональные антитела, которые узнают и элиминируют клоны Т и В-клеток, обусловливающие патогенез аутоиммунного заболевания. Поиск аутореактивных клонов является сложной и актуальной задачей современной биомедицины.

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2

Choreño-Parra, José Alberto, Martha Carnalla-Cortés, Nayeli Martínez-Zúñiga, and Parménides Guadarrama-Ortíz. "Anticuerpos monoclonales contra el CGRP para el tratamiento de la migraña crónica y episódica." Revista Mexicana de Neurociencia 19, no. 4 (July 1, 2018): 45–61. http://dx.doi.org/10.31190/rmn.2018.19.4.45.61.

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3

Sela, Michael. "ON THE NOTION OF SYNERGY OF MONOCLONAL ANTIBODIES AS DRUGS." Biotechnologia Acta 6, no. 4 (2013): 16–19. http://dx.doi.org/10.15407/biotech6.04.016.

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4

Reschova, S., D. Pokorova, Z. Nevorankova, J. Hulova, and T. Vesely. "Detection of spring viraemia of carp virus (SVCV) with monoclonal antibodies." Veterinární Medicína 52, No. 7 (January 7, 2008): 308–16. http://dx.doi.org/10.17221/2043-vetmed.

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Monoclonal antibodies (MAbs) against spring viraemia of carp virus (SVCV), a severe disease in cyprinid fish, were prepared. Nine MAbs were characterised using Western blotting (WB) where all reacted with glycoprotein G, except for MAb 2E1, which showed no reactivity in WB. All nine MAbs showed specificity in an immunoperoxidase test. In ELISA assays, their titres ranged between 1:32 000 and 1:128 000. A panel of SVCV isolates from different European regions were set up and examined by sandwich ELISA assay using the MAbs at a concentration of 15 μg/ml. Only MAb 4C12/3C8 showed low sensitivity in most of the isolates at an absorbance of A<sub>450</sub> the other MAbs, even the lowest absorbance value measured exceeded cut-off for evaluation of the whole reaction. No cross-reaction with the infectious haematopoietic necrosis virus (IHNV), viral haemorrhagic septicaemia virus (VHSV) or infectious pancreatic necrosis virus (IPNV) was demonstrated. 2E1 did not show cross-reactivity with PFRV classified in genogroup III−IV and reacted with a Czech SVCV isolate; its identity was confirmed by means of RT PCR assay. The others MAbs reacted positively with PFRV F4 reference strain, isolated from <i>Esox lucius</i> L. (genogroup III).

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5

Pekárová-Kyněrová, B., and M. Kutíková. "Preparation and use of monoclonal antibodies to detect Phytophthora nicotianae var. nicotianae." Plant Protection Science 35, No. 2 (January 1, 1999): 41–46. http://dx.doi.org/10.17221/9673-pps.

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A monoclonal antibody (MAb 18) was prepared against purified mycelial proteins from Phytophthora nicotianae var. nicotianae. The specificity of MAb 18 (lgG class) was tested using indirect ELISA (PTA-ELISA).It cross-reacted with Phytophthora cacto rum, P. cinrzamomi, P. cryptogea, P. fragariae) but not with other fungi (Fusarium oxysporum, Pythium ultimwn and P. oligan drwn) and bacteria (Clavibacter michiganensis subsp. michiganensis) isolated from tomato. Phytophthora nicotianae var. nicotianae was detected in roots and basal stems of artificially infected young tomato plants using indirect ELISA and immunoprinting.

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6

Reschová, S., D. Pokorová, Z. Nevoránková, and J. Franz. "Monoclonal antibodies to bovine coronavirus and their use in enzymoimmunoanalysis and immunochromatography." Veterinární Medicína 46, No. 5 (January 1, 2001): 125–31. http://dx.doi.org/10.17221/7869-vetmed.

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Two monoclonal antibodies (MAb) to the outer structural protein E2 (spike peplomeric protein) and two MAb to the inner capsid protein N of bovine coronavirus (BCV) were prepared and identified by Western blotting to be used for increasing the specificity and sensitivity of BCV detection. The MAb were checked by the haemagglutination inhibition test and immunoperoxidase tests and no cross reactivity with rotavirus was demonstrated by the immunoperoxidase test and ELISA. A mixture of all the four MAb at predetermined optimum concentrations was first used in sandwich ELISA and then, in combination with an anti‑coronavirus polyclonal antibody, for the development of a simple and rapid immunochromatographic test (ICT). The results of which can be read visually within 10 min. The inclusion of MAb into ELISA and ICT allows the detection of both intact and incomplete BCV virions. ELISA and ICT were used in the examination of a set of 74 faecal samples collected from calves suffering from diarrhoea. ELISA, used as the golden standard verified by electron microscopy, detected BCV in 15 samples (20.3%) and ICT in 16 samples. Three of the ICT‑positive samples were negative by ELISA. On the other hand, two of the 58 ICT‑negative samples were positive by ELISA. Sensitivity and specificity of ICT were 94.9% and 86.7%, respectively

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7

Израельсон, М. А., А. В. Степанов, Д. Б. Староверов, И. А. Шагина, А. К. Мисорин, А. В. Евстратьева, Е. М. Мерзляк, Е. А. Богданова, О. В. Британова, and С. А. Лукьянов. "Тестирование моноклональных антител к Т-клеточному рецептору, ассоциированному с анкилозирующим спондилитом." ПРОФИЛАКТИЧЕСКАЯ МЕДИЦИНА, no. 5 (December 4, 2018): 83–92. http://dx.doi.org/10.24075/vrgmu.2018.064.

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В последние десятилетия в лечении аутоиммунных заболеваний прослеживается тенденция к замещению симптоматической на молекулярно-таргетную терапию. Предпосылками для этого служат как установленные механизмы развития заболевания, так и прогресс в области биотехнологии. Недавно было показано, что Т-клеточные рецепторы, содержащие вариабельные участки β-цепи TRBV9, ассоциированы со спондилоартропатиями, включая анкилозирующий спондилит. Целью данной работы было получение, определение специфичности и оценка цитотоксичности химерного моноклонального антитела, взаимодействующего с вариабельным участком β-цепи Т-клеточного рецептора, который кодируется генным сегментом TRBV9. С помощью цитометрического анализа, а также массированного секвенирования показано, что химерное антитело обладает высокой специфичностью и цитотоксической активностью. Получение лечебного антитела к потенциально патогенному Т-клону может быть перспективным подходом для терапии аутоиммунных заболеваний в целом и АС в частности.

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8

Velez, D., J. D. Macmillan, and L. Miller. "Production and use of monoclonal antibodies for identification of Bradyrhizobium japonicum strains." Canadian Journal of Microbiology 34, no. 1 (January 1, 1988): 88–92. http://dx.doi.org/10.1139/m88-018.

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Thirteen murine hybridomas capable of producing monoclonal antibodies to somatic antigens on Bradyrhizobium japonicum were developed and an indirect enzyme-linked immunosorbent assay was used to test reactivity of the antibodies against 20 strains of B. japonicum. Although polyclonal antisera from mice immunized with strains of B. japonicum reacted with bacterial cells of all 20 strains, individual monoclonals were more specific. Some antibodies reacted with as few as 2 and one with as many as 11 strains. On the basis of reactivity with the set of 13 monoclonal antibodies, the 20 strains of B. japonicum could be divided arbitrarily into five groups. Three of five monoclonal antibodies tested reacted with bacteroids taken directly from soybean nodules. One monoclonal bound to cells of five species of Rhizobium, but none of the 13 reacted with gram-negative bacteria representing six other genera. Treatment of cells with reagents and heat indicated the chemical nature of the antigens to five of the monoclonals. Antigen reactive with one antibody was destroyed by periodate oxidation indicating that it was a polysaccharide. Two antigens were probably proteins as they could be digested by trypsin and denatured by heat. Two others were inactivated by all three treatments suggesting they were glycoproteins.

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9

Vesely, T., S. Reschova, D. Pokorova, J. Hulova, and Z. Nevorankova. "Production of monoclonal antibodies against immunoglobulin heavy chain in common carp (Cyprinus carpio L.)." Veterinární Medicína 51, No. 5 (March 20, 2012): 296–302. http://dx.doi.org/10.17221/5549-vetmed.

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A method for purification of carp serum immunoglobulin (IgM), intended for the production of monoclonal antibodies, was described in the present study. Hybridomas that produce antibodies against IgM heavy chain were selected by ELISA method and Western blotting. Ascitic fluids were prepared and tested by the above mentioned methods, and their typing followed. Monoclonal antibody with the highest titre of antibodies against carp immunoglobulin was selected for conjugation with horseradish peroxidase. Specificity of conjugated monoclonal antibody was tested in a panel of various fish species sera. Cross-reactivity was not detected in rainbow trout (Oncorhynchus mykiss) and eleven other fish species. Besides common carp, positive results were also found in goldfish (Carassius auratus) and bighead carp (Aristichthys nobilis), that are members of Cyprinidae family. Among fish other than Cyprinidae, positive results were also detected in sheatfish (Silurus glanis). The sensitivity in common carp was approximately 10 ng/ml.

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10

Galkin, O. Yu, O. B. Besarab, Yu V. Gorshunov, and O. M. Ivanova. "New monoclonal antibodies to the Chlamydia trachomatis main outer membrane protein and their immunobiological properties." Ukrainian Biochemical Journal 91, no. 3 (May 15, 2019): 90–98. http://dx.doi.org/10.15407/ubj91.03.090.

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11

&NA;. "Monoclonal antibodies." Reactions Weekly &NA;, no. 1293 (March 2010): 36. http://dx.doi.org/10.2165/00128415-201012930-00100.

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12

Melamed, M. D., and C. E. Bradley. "Monoclonal antibodies." Current Opinion in Immunology 1, no. 5 (June 1989): 929–36. http://dx.doi.org/10.1016/0952-7915(89)90075-7.

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13

Koch, C., and J. Bennedsen. "Monoclonal antibodies." Current Opinion in Immunology 2, no. 3 (February 1990): 385–91. http://dx.doi.org/10.1016/0952-7915(89)90146-5.

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14

Chatenoud, L. "Monoclonal antibodies." Current Opinion in Immunology 2, no. 2 (January 1989): 246–48. http://dx.doi.org/10.1016/0952-7915(89)90195-7.

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15

Kosmas, C., H. Kalofonos, and A. A. Epenetos. "Monoclonal Antibodies." Drugs 38, no. 5 (November 1989): 645–57. http://dx.doi.org/10.2165/00003495-198938050-00001.

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16

Rieger, Paula Trahan. "Monoclonal Antibodies." American Journal of Nursing 87, no. 4 (April 1987): 469. http://dx.doi.org/10.2307/3470440.

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17

Buchsbaum, Donald J. "Monoclonal antibodies." International Journal of Radiation Oncology*Biology*Physics 17 (January 1989): 84–85. http://dx.doi.org/10.1016/0360-3016(89)90573-7.

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18

Carter, Philip B., Kim Holly Beegle, and Douglas H. Gebhard. "Monoclonal Antibodies." Veterinary Clinics of North America: Small Animal Practice 16, no. 6 (November 1986): 1171–79. http://dx.doi.org/10.1016/s0195-5616(86)50135-2.

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19

Mulshine, James. "Monoclonal Antibodies." Chest 89, no. 4 (April 1986): 355S. http://dx.doi.org/10.1378/chest.89.4_supplement.355s.

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20

Rosen, Steven T., Elyse A. Lambiase, Yixing Ma, James A. Radosevich, and Alan L. Epstein. "Monoclonal antibodies." Postgraduate Medicine 77, no. 4 (March 1985): 129–34. http://dx.doi.org/10.1080/00325481.1985.11698922.

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21

Rabin, Brace S. "Monoclonal antibodies." Postgraduate Medicine 79, no. 1 (January 1986): 293–303. http://dx.doi.org/10.1080/00325481.1986.11699254.

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22

&NA;. "Monoclonal Antibodies." Journal of Pediatric Hematology/Oncology 25, no. 4 (April 2003): S5—S6. http://dx.doi.org/10.1097/00043426-200304000-00025.

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23

&NA;. "Monoclonal Antibodies." Journal of Pediatric Hematology/Oncology 25, no. 4 (April 2003): S17—S18. http://dx.doi.org/10.1097/00043426-200304000-00036.

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24

Anderson, Philip O. "Monoclonal Antibodies." Breastfeeding Medicine 11, no. 3 (April 2016): 100–101. http://dx.doi.org/10.1089/bfm.2016.0026.

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25

Cowden, Jessica, and Sarah K. Parker. "Monoclonal Antibodies." Pediatric Infectious Disease Journal 25, no. 6 (June 2006): 553–55. http://dx.doi.org/10.1097/01.inf.0000223443.80696.5b.

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26

Ghobrial, Rafik M., Ronald W. Busuttil, and Jerzy W. Kupiec-Weglinski. "Monoclonal antibodies." Current Opinion in Organ Transplantation 2, no. 1 (October 1997): 82–88. http://dx.doi.org/10.1097/00075200-199710000-00015.

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27

La Pine, Timothy R., and Harry R. Hill. "Monoclonal antibodies." Seminars in Pediatric Infectious Diseases 12, no. 1 (January 2001): 64–70. http://dx.doi.org/10.1053/spid.2001.19241.

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28

Buchsbaum, Donald J. "Monoclonal antibodies." International Journal of Radiation Oncology*Biology*Physics 19 (January 1990): 92. http://dx.doi.org/10.1016/0360-3016(90)90591-7.

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29

Buchsbaum, Donald J. "Monoclonal antibodies." International Journal of Radiation Oncology*Biology*Physics 21 (January 1991): 82. http://dx.doi.org/10.1016/0360-3016(91)90373-c.

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30

Drakeman, Donald L., and Paul K. Wallace. "Monoclonal antibodies." Emerging Drugs 4, no. 1 (January 1999): 355–65. http://dx.doi.org/10.1517/14728214.4.1.355.

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31

Nowak, Thomas P. "Monoclonal Antibodies." American Journal of Clinical Oncology 10, no. 4 (August 1987): 278–80. http://dx.doi.org/10.1097/00000421-198708000-00002.

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32

Geskin, Larisa J. "Monoclonal Antibodies." Dermatologic Clinics 33, no. 4 (October 2015): 777–86. http://dx.doi.org/10.1016/j.det.2015.05.015.

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33

Borek, F. "Monoclonal antibodies." Journal of Immunological Methods 77, no. 1 (February 1985): 175. http://dx.doi.org/10.1016/0022-1759(85)90197-8.

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34

Howland, J. L. "Monoclonal antibodies." Biochemical Education 23, no. 4 (October 1995): 223. http://dx.doi.org/10.1016/0307-4412(95)90177-9.

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35

Carron, Christopher P., H. Ward Jarvis, and Patricia M. Saling. "Characterization of Antibodies to Idiotypic Determinants of Monoclonal Anti-Sperm Antibodies1." Biology of Reproduction 38, no. 5 (June 1, 1988): 1093–103. http://dx.doi.org/10.1095/biolreprod38.5.1093.

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36

Sellwood, Jane, and Lynn Smith. "Rapid Detection of Poliovirus from Waters Using Monoclonal Antibodies." Water Science and Technology 21, no. 3 (March 1, 1989): 299–301. http://dx.doi.org/10.2166/wst.1989.0123.

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Poliovirus is present in many types of water in the environment. A rapid detection method for the presence of Poliovirus could be relevant to water management. Virus components are present in cell culture from 6-18 hours after infection. The indirect immunofluorescent staining technique can be used to detect the components. Monoclonal antibodies may provide specific and sensitive reagents for this test. Two of over 50 mouse monoclonal antibodies screened were able to recognise and attach to Poliovirus 3 infected cells. The time at which fluorescence was detected was dependent on the initial virus concentration. These two monoclonals recognise ‘early' produced structural protein before its configuration into a mature capsid.

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37

Hanna, R. E. B., A. G. Trudgett, and A. Anderson. "Fasciola hepatica: development of monoclonal antibodies against somatic antigens and their characterization by ultrastructural localization of antibody binding." Journal of Helminthology 62, no. 1 (March 1988): 15–28. http://dx.doi.org/10.1017/s0022149x00011147.

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ABSTRACTA series of monoclonal antibodies was prepared against tegumental and internal antigens ofFasciola hepaticaby immunizing mice with whole adult-fluke homogenates prior to harvesting the splenic lymphocytes for fusion. Preliminary screening by the Indirect Fluorescent Antibody technique indicated the occurrence of discrete groups of monoclonals differing from one another in tissue-specificity but within which IFA labelling patterns were fairly consistent. Representative hybridomas for 5 of these groups were stabilized and used to produce ascites fluid in mice. By application of an immunogold labelling technique it was possible to map the distribution of antigens for which each monoclonal antibody had affinity throughout the tissues of 4-week and 12-week flukes. Several monoclonals specifically labelled antigenic determinants on the important tegumental antigen T1. However the distribution of gold colloid labelling suggested that epitopes other than that normally exposed to the infected host were recognized; and several monoclonals specifically attached to T1 antigen in the tegument of juvenile worms only. The glycocalyx of the gut and excretory system of flukes shared T1 antigenicity with the tegument. Monoclonal antibodies were produced against an internal immunogen associated with ribosomes and heterochromatin in active protein-producing cells, and against interstitial material of adult flukes. Monoclonals against antigens in parenchymal cell cytoplasm and in mature vitelline cells were recognized but the corresponding hybridomas were not stabilized.

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38

Linhardt, Robert J., C. W. Abell, R. M. Denney, B. W. Altrock, R. Auerbach, S. D. Bernal, R. E. Canfield, et al. "Monoclonal antibodies and immobilized antibodies." Applied Biochemistry and Biotechnology 15, no. 1 (June 1987): 53–80. http://dx.doi.org/10.1007/bf02798506.

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39

Singh, Vinod. "Structural requirement for the recognition of luteinizing hormone releasing hormone (LHRH) by monoclonal and conventional anti-LHRH antibodies." Biochemistry and Cell Biology 64, no. 12 (December 1, 1986): 1372–77. http://dx.doi.org/10.1139/o86-180.

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Immunochemical studies on monoclonal and conventional anti-LHRH antibodies have been reported. The association constants (Ka) were in the order of 109–1010 L/mol when calculated from Scatchard and Steward–Petty plots. Heterogeneity indices (a) calculated from Sips plot were nearly 1.0, indicating the homogeneous nature of monoclonals. Most of the conventional anti-LHRH produced by monkey, baboon, rabbit, and dog, by immunization using LHRH linked to tetanus toxoid by the carbodiimide condensation method, showed a single slope in Scatchard analysis (except two dog antisera) and a values were nearly 1.0. Monoclonals and conventionals reacted most strongly with native LHRH(NH2). Monoclonals showed poor reactivity with LHRH free acid and LHRH fragments containing free acid. The C-terminus tetrapeptide 7–10 showed 10 times more reactivity than tripeptide 4–6. The heptapeptide 4–10 showed 100 and 1000 times more reactivity than the tetra- and tri-peptide, respectively. Introduction of the tripeptide pGlu-His-Trp-OH to heptapeptide 4–10 caused five times more inhibition in reactivity than the heptapeptide. Conventional anti-LHRH antibodies manifested specificity to the C-terminus of LHRH. These sera did not react with LHRH free acid and LHRH fragments of sequence 4–6, 7–10, and 4–10. The complete loss of reactivity of conventional antibodies and poor reactivity of monoclonal antibodies was partly regained when LHRH free acid was coupled to Lys, Lys-MDP, or (Ala)2-tuftsin, suggesting that for monoclonals and conventionals the antigenic determinant was confined to the conformation involving the C-terminus amide of LHRH.

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40

Gidney, M. A. J., D. R. Bundle, A. Godard, and B. W. Griffiths. "Development and characterization of monoclonal antibodies to pregnancy-specific β1-glycoprotein." Canadian Journal of Biochemistry and Cell Biology 63, no. 7 (July 1, 1985): 737–42. http://dx.doi.org/10.1139/o85-092.

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Six monoclonal antibodies were developed to pregnancy-specific β1-glycoprotein (PSβ1G). Studies of ascitic fluid antibodies by a double-antibody radioimmunoassay (RIA) included an evaluation of titers, dose–response parameters, and mass action properties. Four of the antibodies demonstrated moderate to high titers ranging from 1/40 000 to > 1/120 000, as determined by the specific binding of 125I-labeled PSβ1G. In inhibition studies utilizing a standard containing known quantities of placental PSβ1G, two of the antibodies (AR#11 and B#2) were highly sensitive and only slightly lower in this regard than a high affinity polyclonal antiserum. The binding affinities of AR#11 and B#2 monoclonals were greater than 109 mol−1 which underline their importance as potential clinical reagents for the RIA of PSβ1G. The Scatchard plots, for several of the antibodies, were linear and in full agreement with a single order of binding sites predicted for specific monoclonal reagents. Immunodiffusion results provide preliminary evidence that at least three distinct determinants on PSβ1G are recognized by a number of the monoclonal antibodies. Further studies on the fine specificities of the antibodies by solid-phase RIA, as well as a detailed evaluation of their clinical applications, are in progress.

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41

Vass, M., L. Kotkova, I. Diblikova, Z. Nevorankova, Cooper KM, Kennedy DG, and M. Franek. "Production and characterisation of monoclonal antibodies for the detection of AOZ, a tissue bound metabolite of furazolidone." Veterinární Medicína 50, No. 7 (March 28, 2012): 300–310. http://dx.doi.org/10.17221/5627-vetmed.

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3-amino-2-oxazolidinone (AOZ) is a tissue bound toxic metabolite derived from the nitrofuran antibiotic, furazolidone. AOZ is detected in the derivatised form of 3-{[(2-nitrophenyl) methylene] amino}-2-oxa-zolidinone (NP AOZ). 3-{[(3-carboxyphenyl)-methylene] amino-2-oxazolidinone (CP AOZ) was used as the immunising hapten for the production of monoclonal antibodies against NP AOZ. Monoclonal antibodies were produced using hybridomas from the fusion of murine myeloma cells and spleen cells isolated from BALB/c mice immunised with CP AOZ-ethylenediamine-human serum albumin (CP AOZ-ed-HSA). The antibody production in ascitic fluids from clones 3B8/2B9 and 2D11/A4 was monitored during a 16 month period. Repeated cultures of these hybridomas, followed by injection into mice and cloning did not change the assay parameters. Clone 2D11/A4 exhibited long term stability in antibody production throughout the experiment whereas clone 3B8/2B9 demonstrated variability in particular antibody yields whilst retaining assay sensitivity. Reasons for this production variability in clones are discussed. In an optimised direct ELISA format, the antibodies exhibited a 50% binding inhibition in the range of 0.52–1.15 ng/ml with NP AOZ (0.22 -0.50 ng/ml, respective AOZ equivalents) and showed high specificity towards this analyte. The sensitivity of monoclonal antibodies incorporated into the ELISA is compatible with the European Union MRLP and is currently in use for routine analysis.

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42

&NA;. "Antineoplastics/monoclonal antibodies." Reactions Weekly &NA;, no. 1227 (November 2008): 5–6. http://dx.doi.org/10.2165/00128415-200812270-00016.

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43

Yamada, Taketo. "Therapeutic Monoclonal Antibodies." Keio Journal of Medicine 60, no. 2 (2011): 37–46. http://dx.doi.org/10.2302/kjm.60.37.

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44

Susla, Gregory M., and Richard B. Dew. "Antiendotoxin Monoclonal Antibodies." Drug Safety 11, no. 4 (October 1994): 215–22. http://dx.doi.org/10.2165/00002018-199411040-00001.

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45

Brumley, Cindy L., and Joseph A. Kuhn. "Radiolabeled Monoclonal Antibodies." AORN Journal 62, no. 3 (September 1995): 341–55. http://dx.doi.org/10.1016/s0001-2092(06)63575-8.

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Suter, Mark. "Rabbit monoclonal antibodies." Pharmacological Research 22 (September 1990): 473. http://dx.doi.org/10.1016/s1043-6618(09)80477-5.

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Breedveld, FC. "Therapeutic monoclonal antibodies." Lancet 355, no. 9205 (February 2000): 735–40. http://dx.doi.org/10.1016/s0140-6736(00)01034-5.

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Houghton, Alan N. "Raising Monoclonal Antibodies." Cell 96, no. 4 (February 1999): 458–59. http://dx.doi.org/10.1016/s0092-8674(00)80635-2.

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Costanzo, Maria Rosa. "New monoclonal antibodies." Current Opinion in Cardiology 11, no. 2 (March 1996): 204–7. http://dx.doi.org/10.1097/00001573-199603000-00014.

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Rossi, Sabrina, Licia Laurino, Alberto Furlanetto, Serena Chinellato, Enrico Orvieto, Fabio Canal, Fabio Facchetti, and Angelo P. Dei Tos. "Rabbit Monoclonal Antibodies." American Journal of Clinical Pathology 124, no. 2 (August 2005): 295–302. http://dx.doi.org/10.1309/nr8hn08gdpvemu08.

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